ID A0A1Y2K211_9PROT Unreviewed; 555 AA.
AC A0A1Y2K211;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Putative oxaloacetate decarboxylase {ECO:0000313|EMBL:OSM02058.1};
GN ORFNames=MAIT1_05368 {ECO:0000313|EMBL:OSM02058.1};
OS Magnetofaba australis IT-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Magnetococcales;
OC Magnetococcaceae; Magnetofaba.
OX NCBI_TaxID=1434232 {ECO:0000313|EMBL:OSM02058.1, ECO:0000313|Proteomes:UP000194003};
RN [1] {ECO:0000313|EMBL:OSM02058.1, ECO:0000313|Proteomes:UP000194003}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IT-1 {ECO:0000313|EMBL:OSM02058.1,
RC ECO:0000313|Proteomes:UP000194003};
RX PubMed=27801294; DOI=10.1186/s12864-016-3064-9;
RA Araujo A.C., Morillo V., Cypriano J., Teixeira L.C., Leao P., Lyra S.,
RA Almeida L.G., Bazylinski D.A., Vasconcellos A.T., Abreu F., Lins U.;
RT "Combined genomic and structural analyses of a cultured magnetotactic
RT bacterium reveals its niche adaptation to a dynamic environment.";
RL BMC Genomics 17:726-726(2016).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OSM02058.1}.
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DR EMBL; LVJN01000020; OSM02058.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2K211; -.
DR STRING; 1434232.MAIT1_05368; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000194003; Unassembled WGS sequence.
DR GO; GO:0004736; F:pyruvate carboxylase activity; IEA:UniProt.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR CDD; cd06850; biotinyl_domain; 1.
DR CDD; cd07937; DRE_TIM_PC_TC_5S; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001882; Biotin_BS.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR003379; Carboxylase_cons_dom.
DR InterPro; IPR000891; PYR_CT.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR45266; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1.
DR PANTHER; PTHR45266:SF3; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR Pfam; PF02436; PYC_OADA; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF89000; post-HMGL domain-like; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 4: Predicted;
KW Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Reference proteome {ECO:0000313|Proteomes:UP000194003}.
FT DOMAIN 4..266
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 482..555
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 555 AA; 60215 MW; 82B1C4255891C24D CRC64;
MSKLGITELA LRDAHQSLLA TRMRIEDMLP IAPKMDEIGF WSIEAWGGAT FDSCIRFLGE
DPWERARLLK KAMPKTPLQM LFRGQNILGY RHYADDVVEA FVERAYANGI EVFRIFDAMN
DTRNLETAIK ATLKIGGTAH AQGTLSYTIS DVHTIDMWVD MAKKLEDMGS HSICIKDMAG
LLKPYVGEEL VTRLKEAVSV PIAMQCHATT GLSTATIVKC AEAGIDMVDT ATASMSMTYG
HSATESVVSI LEGTERDTGL NLQALEEVSA YFRKVRPKYK KFEGSLKGVD SRILIAQVPG
GMLTNMENQL KQQGAGDRMD EVLEEIPRVR KDLGTIALVT PTSQIVGTQA VFNVLMGERY
KTITKETRGI LRGEYGATPG PMNKELQARV LEEGEKPITC RPADLLQPEL DKLTAELKGL
AAEKNIKLAE AEIDDVLTYA LFPQVGLKFL QNRDNPDAFE PAPWLEEEPK PAAAPAAPAA
APAASGAPVN APLAGNVVKV KVAVGETVAS GDVIVVLEAM KMETEVRAPR GGSVTAIHIS
EGKAVNLGDP LLDLA
//
